HEADER TRANSFERASE 16-OCT-06 2IRU
TITLE CRYSTAL STRUCTURE OF THE POLYMERASE DOMAIN FROM MYCOBACTERIUM
TITLE 2 TUBERCULOSIS LIGASE D
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE DNA LIGASE-LIKE PROTEIN RV0938/MT0965;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LIGD POLYMERASE DOMAIN (RESIDUES 1-300);
COMPND 5 EC: 2.7.7.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: RV098;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS POLYMERASE, PRIMASE, LIGASE, NHEJ, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.C.BRISSETT,R.S.PITCHER,A.J.DOHERTY
REVDAT 4 13-JUL-11 2IRU 1 VERSN
REVDAT 3 24-FEB-09 2IRU 1 VERSN
REVDAT 2 30-OCT-07 2IRU 1 JRNL
REVDAT 1 02-JAN-07 2IRU 0
JRNL AUTH R.S.PITCHER,N.C.BRISSETT,A.J.PICHER,P.ANDRADE,R.JUAREZ,
JRNL AUTH 2 D.THOMPSON,G.C.FOX,L.BLANCO,A.J.DOHERTY
JRNL TITL STRUCTURE AND FUNCTION OF A MYCOBACTERIAL NHEJ DNA REPAIR
JRNL TITL 2 POLYMERASE.
JRNL REF J.MOL.BIOL. V. 366 391 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17174332
JRNL DOI 10.1016/J.JMB.2006.10.046
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.9
REMARK 3 NUMBER OF REFLECTIONS : 60313
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3237
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3268
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 66.96
REMARK 3 BIN R VALUE (WORKING SET) : 0.3330
REMARK 3 BIN FREE R VALUE SET COUNT : 192
REMARK 3 BIN FREE R VALUE : 0.4670
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4344
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 663
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 20.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.65000
REMARK 3 B22 (A**2) : -0.21000
REMARK 3 B33 (A**2) : -0.45000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.12000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.117
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.120
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.066
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.540
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4444 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6069 ; 1.478 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 566 ; 6.097 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 181 ;30.814 ;22.597
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 698 ;13.589 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;19.880 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 700 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3380 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2267 ; 0.215 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3055 ; 0.302 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 479 ; 0.260 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 46 ; 0.198 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 23 ; 0.247 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2907 ; 0.924 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4579 ; 1.430 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1754 ; 2.269 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1490 ; 3.382 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 6 A 114
REMARK 3 ORIGIN FOR THE GROUP (A): -1.9560 43.6160 21.8590
REMARK 3 T TENSOR
REMARK 3 T11: 0.0263 T22: 0.0267
REMARK 3 T33: 0.0359 T12: -0.0048
REMARK 3 T13: -0.0022 T23: 0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 0.7723 L22: 0.9954
REMARK 3 L33: 1.3342 L12: 0.0915
REMARK 3 L13: 0.1683 L23: 0.2552
REMARK 3 S TENSOR
REMARK 3 S11: -0.0119 S12: 0.0165 S13: -0.0467
REMARK 3 S21: -0.1016 S22: -0.0107 S23: 0.0177
REMARK 3 S31: 0.0220 S32: -0.0859 S33: 0.0225
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 115 A 208
REMARK 3 ORIGIN FOR THE GROUP (A): -2.9670 22.0650 32.9130
REMARK 3 T TENSOR
REMARK 3 T11: 0.1261 T22: -0.0189
REMARK 3 T33: 0.0374 T12: -0.0205
REMARK 3 T13: -0.0230 T23: 0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 1.3809 L22: 1.4390
REMARK 3 L33: 2.3692 L12: 0.3404
REMARK 3 L13: 0.0722 L23: -1.4353
REMARK 3 S TENSOR
REMARK 3 S11: 0.0451 S12: -0.0488 S13: -0.1058
REMARK 3 S21: -0.1330 S22: -0.0107 S23: -0.0710
REMARK 3 S31: 0.4484 S32: -0.0866 S33: -0.0344
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 209 A 261
REMARK 3 ORIGIN FOR THE GROUP (A): -5.3180 29.6690 39.4370
REMARK 3 T TENSOR
REMARK 3 T11: 0.0783 T22: 0.0387
REMARK 3 T33: 0.0059 T12: -0.0425
REMARK 3 T13: -0.0233 T23: 0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 0.1869 L22: 1.3638
REMARK 3 L33: 1.0002 L12: -0.0450
REMARK 3 L13: -0.0830 L23: -1.1216
REMARK 3 S TENSOR
REMARK 3 S11: 0.0218 S12: -0.1082 S13: -0.0098
REMARK 3 S21: 0.1396 S22: 0.0869 S23: 0.0904
REMARK 3 S31: 0.1171 S32: -0.2243 S33: -0.1087
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 262 A 291
REMARK 3 ORIGIN FOR THE GROUP (A): 10.8030 34.2470 37.1140
REMARK 3 T TENSOR
REMARK 3 T11: 0.0105 T22: 0.0015
REMARK 3 T33: 0.0108 T12: 0.0145
REMARK 3 T13: -0.0532 T23: 0.0430
REMARK 3 L TENSOR
REMARK 3 L11: 3.2355 L22: 2.9856
REMARK 3 L33: 1.2636 L12: 1.0968
REMARK 3 L13: 0.6539 L23: -0.2056
REMARK 3 S TENSOR
REMARK 3 S11: 0.1135 S12: -0.3510 S13: -0.2024
REMARK 3 S21: 0.2722 S22: -0.0844 S23: -0.3848
REMARK 3 S31: 0.1560 S32: 0.1365 S33: -0.0291
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 10 B 115
REMARK 3 ORIGIN FOR THE GROUP (A): -22.3600 59.6000 25.1050
REMARK 3 T TENSOR
REMARK 3 T11: 0.0156 T22: 0.0314
REMARK 3 T33: 0.0311 T12: -0.0231
REMARK 3 T13: -0.0074 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.6343 L22: 1.1062
REMARK 3 L33: 1.3674 L12: -0.0205
REMARK 3 L13: -0.0430 L23: 0.2140
REMARK 3 S TENSOR
REMARK 3 S11: 0.0231 S12: -0.0683 S13: 0.0281
REMARK 3 S21: 0.1008 S22: -0.0560 S23: 0.0815
REMARK 3 S31: -0.0440 S32: -0.0307 S33: 0.0328
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 116 B 162
REMARK 3 ORIGIN FOR THE GROUP (A): -21.1900 78.9110 17.6130
REMARK 3 T TENSOR
REMARK 3 T11: 0.1291 T22: 0.0243
REMARK 3 T33: 0.0700 T12: -0.0359
REMARK 3 T13: -0.0104 T23: -0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 1.5307 L22: 2.1878
REMARK 3 L33: 4.3759 L12: -0.1315
REMARK 3 L13: -0.1748 L23: -1.8199
REMARK 3 S TENSOR
REMARK 3 S11: 0.0709 S12: 0.0450 S13: 0.0378
REMARK 3 S21: 0.1115 S22: -0.0625 S23: 0.0138
REMARK 3 S31: -0.2475 S32: 0.1492 S33: -0.0084
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 163 B 190
REMARK 3 ORIGIN FOR THE GROUP (A): -16.2290 81.1390 15.4280
REMARK 3 T TENSOR
REMARK 3 T11: 0.1237 T22: 0.0088
REMARK 3 T33: 0.0102 T12: -0.0957
REMARK 3 T13: -0.0032 T23: 0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 1.5418 L22: 8.1237
REMARK 3 L33: 1.6953 L12: -1.1504
REMARK 3 L13: -0.2552 L23: 1.2260
REMARK 3 S TENSOR
REMARK 3 S11: 0.0311 S12: -0.0574 S13: 0.1298
REMARK 3 S21: 0.1693 S22: -0.0798 S23: -0.0695
REMARK 3 S31: -0.3700 S32: 0.0929 S33: 0.0487
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 191 B 223
REMARK 3 ORIGIN FOR THE GROUP (A): -28.0090 85.4810 8.0680
REMARK 3 T TENSOR
REMARK 3 T11: 0.0704 T22: 0.0002
REMARK 3 T33: 0.0159 T12: 0.0166
REMARK 3 T13: 0.0180 T23: 0.0337
REMARK 3 L TENSOR
REMARK 3 L11: 0.9026 L22: 1.7663
REMARK 3 L33: 14.6893 L12: -0.2002
REMARK 3 L13: -0.0057 L23: -2.8035
REMARK 3 S TENSOR
REMARK 3 S11: 0.0310 S12: 0.1191 S13: 0.0743
REMARK 3 S21: 0.1811 S22: 0.1854 S23: 0.1968
REMARK 3 S31: 0.0138 S32: -0.6701 S33: -0.2164
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 224 B 291
REMARK 3 ORIGIN FOR THE GROUP (A): -14.7180 70.3430 12.1320
REMARK 3 T TENSOR
REMARK 3 T11: 0.0222 T22: 0.0296
REMARK 3 T33: 0.0040 T12: -0.0425
REMARK 3 T13: 0.0029 T23: 0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 0.8095 L22: 1.4151
REMARK 3 L33: 1.4580 L12: -0.6366
REMARK 3 L13: 0.1336 L23: -0.3322
REMARK 3 S TENSOR
REMARK 3 S11: 0.0481 S12: 0.1232 S13: 0.0829
REMARK 3 S21: -0.1138 S22: -0.0853 S23: -0.1147
REMARK 3 S31: -0.1779 S32: 0.1724 S33: 0.0372
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2IRU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-06.
REMARK 100 THE RCSB ID CODE IS RCSB039937.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-AUG-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54180
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63571
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 20.370
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.700
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.1
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : 0.02900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.23500
REMARK 200 R SYM FOR SHELL (I) : 0.12900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2 M MG ACETATE, PH
REMARK 280 7.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 285K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 37.89800
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 1
REMARK 465 SER A 2
REMARK 465 HIS A 3
REMARK 465 MET A 4
REMARK 465 GLY A 5
REMARK 465 ALA A 292
REMARK 465 ASP A 293
REMARK 465 ALA A 294
REMARK 465 PRO A 295
REMARK 465 VAL A 296
REMARK 465 ALA A 297
REMARK 465 ASP A 298
REMARK 465 ARG A 299
REMARK 465 LEU A 300
REMARK 465 THR A 301
REMARK 465 ARG A 302
REMARK 465 TYR A 303
REMARK 465 GLY B 1
REMARK 465 SER B 2
REMARK 465 HIS B 3
REMARK 465 MET B 4
REMARK 465 GLY B 5
REMARK 465 SER B 6
REMARK 465 ALA B 7
REMARK 465 SER B 8
REMARK 465 GLU B 9
REMARK 465 ALA B 292
REMARK 465 ASP B 293
REMARK 465 ALA B 294
REMARK 465 PRO B 295
REMARK 465 VAL B 296
REMARK 465 ALA B 297
REMARK 465 ASP B 298
REMARK 465 ARG B 299
REMARK 465 LEU B 300
REMARK 465 THR B 301
REMARK 465 ARG B 302
REMARK 465 TYR B 303
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CE LYS B 55 O HOH B 496 1.94
REMARK 500 NH1 ARG A 11 O HOH A 525 2.10
REMARK 500 O PRO B 189 O HOH B 601 2.13
REMARK 500 O HOH B 513 O HOH B 555 2.14
REMARK 500 CD ARG B 160 O HOH B 495 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 487 O HOH B 359 1655 2.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 54 CG - CD - NE ANGL. DEV. = -12.8 DEGREES
REMARK 500 ARG B 54 CD - NE - CZ ANGL. DEV. = 12.6 DEGREES
REMARK 500 ARG B 54 NE - CZ - NH1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ARG B 54 NE - CZ - NH2 ANGL. DEV. = -8.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 97 15.77 -144.02
REMARK 500 SER A 177 -94.62 -107.24
REMARK 500 LYS A 178 -33.70 -133.66
REMARK 500 THR A 219 107.42 -23.67
REMARK 500 TYR A 244 -7.01 74.20
REMARK 500 SER B 88 -72.58 -71.31
REMARK 500 ASP B 97 17.79 -146.08
REMARK 500 SER B 177 -105.92 -106.34
REMARK 500 THR B 219 133.53 -39.20
REMARK 500 TYR B 244 -5.64 75.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 427 DISTANCE = 5.13 ANGSTROMS
REMARK 525 HOH A 474 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH A 514 DISTANCE = 5.32 ANGSTROMS
REMARK 525 HOH B 447 DISTANCE = 5.18 ANGSTROMS
REMARK 525 HOH B 471 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH B 570 DISTANCE = 5.11 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2IRX RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH GTP.
REMARK 900 RELATED ID: 2IRY RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH DGTP.
DBREF 2IRU A 4 303 UNP P71571 Y938_MYCTU 1 300
DBREF 2IRU B 4 303 UNP P71571 Y938_MYCTU 1 300
SEQADV 2IRU GLY A 1 UNP P71571 EXPRESSION TAG
SEQADV 2IRU SER A 2 UNP P71571 EXPRESSION TAG
SEQADV 2IRU HIS A 3 UNP P71571 EXPRESSION TAG
SEQADV 2IRU GLY B 1 UNP P71571 EXPRESSION TAG
SEQADV 2IRU SER B 2 UNP P71571 EXPRESSION TAG
SEQADV 2IRU HIS B 3 UNP P71571 EXPRESSION TAG
SEQRES 1 A 303 GLY SER HIS MET GLY SER ALA SER GLU GLN ARG VAL THR
SEQRES 2 A 303 LEU THR ASN ALA ASP LYS VAL LEU TYR PRO ALA THR GLY
SEQRES 3 A 303 THR THR LYS SER ASP ILE PHE ASP TYR TYR ALA GLY VAL
SEQRES 4 A 303 ALA GLU VAL MET LEU GLY HIS ILE ALA GLY ARG PRO ALA
SEQRES 5 A 303 THR ARG LYS ARG TRP PRO ASN GLY VAL ASP GLN PRO ALA
SEQRES 6 A 303 PHE PHE GLU LYS GLN LEU ALA LEU SER ALA PRO PRO TRP
SEQRES 7 A 303 LEU SER ARG ALA THR VAL ALA HIS ARG SER GLY THR THR
SEQRES 8 A 303 THR TYR PRO ILE ILE ASP SER ALA THR GLY LEU ALA TRP
SEQRES 9 A 303 ILE ALA GLN GLN ALA ALA LEU GLU VAL HIS VAL PRO GLN
SEQRES 10 A 303 TRP ARG PHE VAL ALA GLU PRO GLY SER GLY GLU LEU ASN
SEQRES 11 A 303 PRO GLY PRO ALA THR ARG LEU VAL PHE ASP LEU ASP PRO
SEQRES 12 A 303 GLY GLU GLY VAL MET MET ALA GLN LEU ALA GLU VAL ALA
SEQRES 13 A 303 ARG ALA VAL ARG ASP LEU LEU ALA ASP ILE GLY LEU VAL
SEQRES 14 A 303 THR PHE PRO VAL THR SER GLY SER LYS GLY LEU HIS LEU
SEQRES 15 A 303 TYR THR PRO LEU ASP GLU PRO VAL SER SER ARG GLY ALA
SEQRES 16 A 303 THR VAL LEU ALA LYS ARG VAL ALA GLN ARG LEU GLU GLN
SEQRES 17 A 303 ALA MET PRO ALA LEU VAL THR SER THR MET THR LYS SER
SEQRES 18 A 303 LEU ARG ALA GLY LYS VAL PHE VAL ASP TRP SER GLN ASN
SEQRES 19 A 303 SER GLY SER LYS THR THR ILE ALA PRO TYR SER LEU ARG
SEQRES 20 A 303 GLY ARG THR HIS PRO THR VAL ALA ALA PRO ARG THR TRP
SEQRES 21 A 303 ALA GLU LEU ASP ASP PRO ALA LEU ARG GLN LEU SER TYR
SEQRES 22 A 303 ASP GLU VAL LEU THR ARG ILE ALA ARG ASP GLY ASP LEU
SEQRES 23 A 303 LEU GLU ARG LEU ASP ALA ASP ALA PRO VAL ALA ASP ARG
SEQRES 24 A 303 LEU THR ARG TYR
SEQRES 1 B 303 GLY SER HIS MET GLY SER ALA SER GLU GLN ARG VAL THR
SEQRES 2 B 303 LEU THR ASN ALA ASP LYS VAL LEU TYR PRO ALA THR GLY
SEQRES 3 B 303 THR THR LYS SER ASP ILE PHE ASP TYR TYR ALA GLY VAL
SEQRES 4 B 303 ALA GLU VAL MET LEU GLY HIS ILE ALA GLY ARG PRO ALA
SEQRES 5 B 303 THR ARG LYS ARG TRP PRO ASN GLY VAL ASP GLN PRO ALA
SEQRES 6 B 303 PHE PHE GLU LYS GLN LEU ALA LEU SER ALA PRO PRO TRP
SEQRES 7 B 303 LEU SER ARG ALA THR VAL ALA HIS ARG SER GLY THR THR
SEQRES 8 B 303 THR TYR PRO ILE ILE ASP SER ALA THR GLY LEU ALA TRP
SEQRES 9 B 303 ILE ALA GLN GLN ALA ALA LEU GLU VAL HIS VAL PRO GLN
SEQRES 10 B 303 TRP ARG PHE VAL ALA GLU PRO GLY SER GLY GLU LEU ASN
SEQRES 11 B 303 PRO GLY PRO ALA THR ARG LEU VAL PHE ASP LEU ASP PRO
SEQRES 12 B 303 GLY GLU GLY VAL MET MET ALA GLN LEU ALA GLU VAL ALA
SEQRES 13 B 303 ARG ALA VAL ARG ASP LEU LEU ALA ASP ILE GLY LEU VAL
SEQRES 14 B 303 THR PHE PRO VAL THR SER GLY SER LYS GLY LEU HIS LEU
SEQRES 15 B 303 TYR THR PRO LEU ASP GLU PRO VAL SER SER ARG GLY ALA
SEQRES 16 B 303 THR VAL LEU ALA LYS ARG VAL ALA GLN ARG LEU GLU GLN
SEQRES 17 B 303 ALA MET PRO ALA LEU VAL THR SER THR MET THR LYS SER
SEQRES 18 B 303 LEU ARG ALA GLY LYS VAL PHE VAL ASP TRP SER GLN ASN
SEQRES 19 B 303 SER GLY SER LYS THR THR ILE ALA PRO TYR SER LEU ARG
SEQRES 20 B 303 GLY ARG THR HIS PRO THR VAL ALA ALA PRO ARG THR TRP
SEQRES 21 B 303 ALA GLU LEU ASP ASP PRO ALA LEU ARG GLN LEU SER TYR
SEQRES 22 B 303 ASP GLU VAL LEU THR ARG ILE ALA ARG ASP GLY ASP LEU
SEQRES 23 B 303 LEU GLU ARG LEU ASP ALA ASP ALA PRO VAL ALA ASP ARG
SEQRES 24 B 303 LEU THR ARG TYR
FORMUL 3 HOH *663(H2 O)
HELIX 1 1 THR A 28 ALA A 48 1 21
HELIX 2 2 SER A 98 GLN A 108 1 11
HELIX 3 3 MET A 148 ASP A 165 1 18
HELIX 4 4 SER A 191 MET A 210 1 20
HELIX 5 5 THR A 219 ARG A 223 5 5
HELIX 6 6 TRP A 231 SER A 235 5 5
HELIX 7 7 THR A 259 ASP A 264 1 6
HELIX 8 8 TYR A 273 GLY A 284 1 12
HELIX 9 9 THR B 28 ALA B 48 1 21
HELIX 10 10 SER B 98 GLN B 108 1 11
HELIX 11 11 MET B 148 ILE B 166 1 19
HELIX 12 12 SER B 191 MET B 210 1 20
HELIX 13 13 TRP B 231 SER B 235 5 5
HELIX 14 14 THR B 259 ASP B 265 1 7
HELIX 15 15 SER B 272 GLY B 284 1 13
SHEET 1 A 4 PHE A 66 GLU A 68 0
SHEET 2 A 4 THR A 53 ARG A 56 -1 N ARG A 56 O PHE A 66
SHEET 3 A 4 GLU A 112 VAL A 115 -1 O HIS A 114 N THR A 53
SHEET 4 A 4 THR A 240 ILE A 241 -1 O THR A 240 N VAL A 115
SHEET 1 B 2 SER A 80 VAL A 84 0
SHEET 2 B 2 THR A 91 ILE A 95 -1 O THR A 91 N VAL A 84
SHEET 1 C 4 TRP A 118 ALA A 122 0
SHEET 2 C 4 LEU A 129 PRO A 143 -1 O ASN A 130 N VAL A 121
SHEET 3 C 4 VAL A 227 ASP A 230 -1 O ASP A 230 N ASP A 140
SHEET 4 C 4 VAL A 214 THR A 215 1 N THR A 215 O VAL A 229
SHEET 1 D 5 TRP A 118 ALA A 122 0
SHEET 2 D 5 LEU A 129 PRO A 143 -1 O ASN A 130 N VAL A 121
SHEET 3 D 5 LEU A 180 VAL A 190 -1 O LEU A 180 N LEU A 141
SHEET 4 D 5 PHE A 171 THR A 174 -1 N VAL A 173 O HIS A 181
SHEET 5 D 5 ALA A 256 PRO A 257 -1 O ALA A 256 N THR A 174
SHEET 1 E 2 THR A 253 VAL A 254 0
SHEET 2 E 2 LEU A 271 SER A 272 -1 O LEU A 271 N VAL A 254
SHEET 1 F 4 PHE B 66 GLU B 68 0
SHEET 2 F 4 THR B 53 ARG B 56 -1 N ARG B 54 O GLU B 68
SHEET 3 F 4 GLU B 112 VAL B 115 -1 O HIS B 114 N THR B 53
SHEET 4 F 4 THR B 240 ILE B 241 -1 O THR B 240 N VAL B 115
SHEET 1 G 2 SER B 80 ALA B 85 0
SHEET 2 G 2 THR B 90 ILE B 95 -1 O THR B 91 N VAL B 84
SHEET 1 H 4 TRP B 118 ALA B 122 0
SHEET 2 H 4 LEU B 129 PRO B 143 -1 O ASN B 130 N VAL B 121
SHEET 3 H 4 VAL B 227 ASP B 230 -1 O PHE B 228 N ASP B 142
SHEET 4 H 4 VAL B 214 THR B 215 1 N THR B 215 O VAL B 229
SHEET 1 I 5 TRP B 118 ALA B 122 0
SHEET 2 I 5 LEU B 129 PRO B 143 -1 O ASN B 130 N VAL B 121
SHEET 3 I 5 LEU B 180 VAL B 190 -1 O LEU B 180 N LEU B 141
SHEET 4 I 5 PHE B 171 THR B 174 -1 N VAL B 173 O HIS B 181
SHEET 5 I 5 ALA B 256 PRO B 257 -1 O ALA B 256 N THR B 174
CRYST1 41.053 75.796 96.100 90.00 92.68 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.024359 0.000000 0.001142 0.00000
SCALE2 0.000000 0.013193 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010417 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
